Different Residues on the Surface of the Methanothermobacter thermautotrophicus MCM Helicase Interact with Single- and Double-Stranded DNA
Figure 1
Locations of the amino acids mutated in the study. (a) An alignment of the amino acid sequences of the region of domain C analyzed in the study. The residues mutated are shown in color. Q176 (green), P210 (magenta), G211 (blue), D212 (red), V214 (yellow), G218 (cyan). The accession numbers used are: Methanothermobacter thermautotrophicus, NP_276876; Picrophilus torridus, YP_023995; Methanosarcina mazei, NP_633860; Sulfolobus tokodaii, NP_376352; Archaeoglobus fulgidus, NP_069353; Halobacterium, NP_280836. (b) Side and top views of the three-dimensional structure of the dodecameric N-terminal portion of the M. thermautotrophicus MCM protein (PDB ID: 1LTL [4]) are shown. The mutated residues are highlighted in colors as in (a). (c) Side and top views of the three-dimensional structure of the monomeric N-terminal portion of the M. thermautotrophicus MCM protein (PDB ID: 1LTL [4]) are shown. The mutated residues are highlighted in color as in (a).
